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| | <StructureSection load='4pn0' size='340' side='right'caption='[[4pn0]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='4pn0' size='340' side='right'caption='[[4pn0]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pn0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PN0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pn0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PN0 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pn1|4pn1]]</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pn0 OCA], [https://pdbe.org/4pn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pn0 RCSB], [https://www.ebi.ac.uk/pdbsum/4pn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pn0 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pct1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 CBS 356])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.33 3.1.3.33] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pn0 OCA], [http://pdbe.org/4pn0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pn0 RCSB], [http://www.ebi.ac.uk/pdbsum/4pn0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pn0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CET1_SCHPO CET1_SCHPO]] First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.<ref>PMID:12788946</ref> | + | [https://www.uniprot.org/uniprot/CET1_SCHPO CET1_SCHPO] First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.<ref>PMID:12788946</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cbs 356]] | |
| - | [[Category: Hydrolase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Doamekpor, S K]] | + | [[Category: Schizosaccharomyces pombe]] |
| - | [[Category: Lima, C D]] | + | [[Category: Doamekpor SK]] |
| - | [[Category: Dimer]] | + | [[Category: Lima CD]] |
| - | [[Category: Mrna capping]]
| + | |
| - | [[Category: Mrna processing]]
| + | |
| - | [[Category: Mrna triphosphatase]]
| + | |
| - | [[Category: Polynucleotide 5' triphosphatase]]
| + | |
| Structural highlights
Function
CET1_SCHPO First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.[1]
Publication Abstract from PubMed
mRNA capping enzymes are directed to nascent RNA polymerase II (Pol2) transcripts via interactions with the carboxy-terminal domains (CTDs) of Pol2 and transcription elongation factor Spt5. Fission yeast RNA triphosphatase binds to the Spt5 CTD, comprising a tandem repeat of nonapeptide motif TPAWNSGSK. Here we report the crystal structure of a Pct1.Spt5-CTD complex, which revealed two CTD docking sites on the Pct1 homodimer that engage TPAWN segments of the motif. Each Spt5 CTD interface, composed of elements from both subunits of the homodimer, is dominated by van der Waals contacts from Pct1 to the tryptophan of the CTD. The bound CTD adopts a distinctive conformation in which the peptide backbone makes a tight U-turn so that the proline stacks over the tryptophan. We show that Pct1 binding to Spt5 CTD is antagonized by threonine phosphorylation. Our results fortify an emerging concept of an "Spt5 CTD code" in which (i) the Spt5 CTD is structurally plastic and can adopt different conformations that are templated by particular cellular Spt5 CTD receptor proteins; and (ii) threonine phosphorylation of the Spt5 CTD repeat inscribes a binary on-off switch that is read by diverse CTD receptors, each in its own distinctive manner.
Fission yeast RNA triphosphatase reads an Spt5 CTD code.,Doamekpor SK, Schwer B, Sanchez AM, Shuman S, Lima CD RNA. 2014 Nov 20. PMID:25414009[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hausmann S, Pei Y, Shuman S. Homodimeric quaternary structure is required for the in vivo function and thermal stability of Saccharomyces cerevisiae and Schizosaccharomyces pombe RNA triphosphatases. J Biol Chem. 2003 Aug 15;278(33):30487-96. Epub 2003 Jun 3. PMID:12788946 doi:http://dx.doi.org/10.1074/jbc.M303060200
- ↑ Doamekpor SK, Schwer B, Sanchez AM, Shuman S, Lima CD. Fission yeast RNA triphosphatase reads an Spt5 CTD code. RNA. 2014 Nov 20. PMID:25414009 doi:http://dx.doi.org/10.1261/rna.048181.114
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